Paxillin (phospho-Ser-83) Blocking Peptide
€155.00
In stock
SKU
ECM-PX1345
Background:
Paxillin, a focal adhesion protein, is involved in focal adhesion formation during cell adhesion and migration. Paxillin contains LD motifs, LIM domains, and SH3-/SH2-binding domains that participate in a variety of protein-protein interactions with kinases, GTPase-activating proteins, and cytoskeletal proteins. Phosphorylation of paxillin occurs at both tyrosine and serine sites. Serine phosphorylation of paxillin occurs in response to growth-factor activation and fibronectins. Both ERK and p38MAPK kinases phosphorylate serine 83 in vitro. HGF stimulation of murine epithelial cells leads to ERK-mediated phosphorylation of Ser-83, which is required for HGF-induced cell spreading and migration. In addition, Ser-83 is phosphorylated in response to NGF in PC12 cells, and this phosphorylation may be involved in neurite extension.
Sequence: Phospho-Paxillin (Ser-83) synthetic peptide corresponds to amino acid residues around serine 83 of mouse paxillin. This sequence is highly conserved in rat and human paxillin and is also found in all isoforms (a, b, g) of paxillin.
Specificity: The peptide is specifically recognized by anti-Paxillin (Ser-83) phospho-specific antibody (PP1341) in ELISA, and has been shown to block the reactivity of PP1341 during Western blot. In addition, the peptide is recommended for use in blocking PP1341 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
Paxillin, a focal adhesion protein, is involved in focal adhesion formation during cell adhesion and migration. Paxillin contains LD motifs, LIM domains, and SH3-/SH2-binding domains that participate in a variety of protein-protein interactions with kinases, GTPase-activating proteins, and cytoskeletal proteins. Phosphorylation of paxillin occurs at both tyrosine and serine sites. Serine phosphorylation of paxillin occurs in response to growth-factor activation and fibronectins. Both ERK and p38MAPK kinases phosphorylate serine 83 in vitro. HGF stimulation of murine epithelial cells leads to ERK-mediated phosphorylation of Ser-83, which is required for HGF-induced cell spreading and migration. In addition, Ser-83 is phosphorylated in response to NGF in PC12 cells, and this phosphorylation may be involved in neurite extension.
Sequence: Phospho-Paxillin (Ser-83) synthetic peptide corresponds to amino acid residues around serine 83 of mouse paxillin. This sequence is highly conserved in rat and human paxillin and is also found in all isoforms (a, b, g) of paxillin.
Specificity: The peptide is specifically recognized by anti-Paxillin (Ser-83) phospho-specific antibody (PP1341) in ELISA, and has been shown to block the reactivity of PP1341 during Western blot. In addition, the peptide is recommended for use in blocking PP1341 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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